CONFORMATIONS OF POLY(ETHYLENE GLYCOL) BOUND HOMO-OLIGO-L-ALANINES AND HOMO-OLIGO-L-VALINES IN AQUEOUS-SOLUTION

被引:61
作者
TONIOLO, C [1 ]
BONORA, GM [1 ]
MUTTER, M [1 ]
机构
[1] UNIV TUBINGEN, INST ORGAN CHEM, D-7400 TUBINGEN 1, FED REP GER
关键词
D O I
10.1021/ja00496a030
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A conformational analysis of poly(ethylene glycol) bound N-tert;-butyloxycarbonylhomooligo-L-alanines and L-valines to the octapeptides was performed in aqueous solution using circular dichroism. It was shown that the alanine and valine peptides may adopt β or statistical coil conformations depending upon chain length, concentration, temperature, ionic strength, presence of the N-blocking group, and pH. In addition, the β structures formed by the valine peptides are more stable than those formed by the corresponding alanine peptides. The origin of the positive dichroism near 215 nm in the homooligo-L-alanines and the effect of mono-and bifunctional poly(ethylene glycol) upon oligopeptide conformation are also discussed. © 1979, American Chemical Society. All rights reserved.
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页码:450 / 454
页数:5
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